Primary amines induce selective release of lysosomal enzymes from mouse macrophages.
Cultured mouse peritoneal macrophages were found to release substantial amounts of lysosomal beta-glucuronidase and beta-glactosidase activites when exposed to millimolar concentrations of various primary aliphatic monoamines. With methylamine, ethylamine, propylamine and butylamine, lysosomal enzyme release was selective, but further increases in the aliphatic chain length resulted in the compounds becoming lytic. By contrast, structurally related primary aliphatic diamines proved to be inactive at inducing both selective and lytic lysosomal-enzyme discharge.
D000588:Amines / Q000494:pharmacology*; D000818:Animals; D001202:Ascitic Fluid / Q000166:cytology; D002478:Cells, Cultured; D005696:Galactosidases / Q000378:metabolism*; D005966:Glucuronidase / Q000378:metabolism*; D008247:Lysosomes / Q000187:drug effects / Q000201:enzymology; D008264:Macrophages / Q000187:drug effects / Q000201:enzymology*; D051379:Mice; D013329:Structure-Activity Relationship; D001616:beta-Galactosidase / Q000378:metabolism*
D000588:Amines; D005696:Galactosidases; D001616:beta-Galactosidase; D005966:Glucuronidase